Autophosphorylation of PTK2:
Autophosphorylation of PTK2 at Y397 creates binding site for CSK, a member of Scr family kinases.
In response to integrin engagement with the ECM, FAK is autophosphorylated predominantly on Y397
This Y397 is the consensus binding site for the SH2 domain of c-Src (CSK)
Interaction of CSK with FAK leads to phosphorylation of FAK on other tyrosine residues including Y407, 576, 577, 861, 925/
These phosphorylation events promote PTK2 to its maximal catalytic activity.
Upon autophosphorylation of FAK, a signaling complex of FAK, CSK binds to and can phosphorylate various adaptor proteins such as p130Cas and paxillin.
e_re980( EMT ):
Src and FAK kinases cooperate to phosphorylate paxillin, stimulate its focal adhesion localization, and regulate cell spreading and protrusiveness.
Phosphorylated paxillin binding to Crk is implicated in Rac activation and stimulation of cell motility
Participates in complexes:
In compartment: Cytoplasm
Participates in reactions:
As Reactant or Product:
- FAK1*|Y_pho|pho|active@Cytoplasm + c-SRC*|Y_pho|active@Cytoplasm → FAK1*|Y_pho|pho:c-SRC*@Cytoplasm
- FAK1*|Y_pho|pho:c-SRC*@Cytoplasm + BCAR1@Cytoplasm + Talin*@Cytoplasm + PXN|pho@Cytoplasm + Vinculin*@Cytoplasm → BCAR1:FAK1*|Y_pho|pho:PXN|pho:Talin*:Vinculin*:c-SRC*@Cytoplasm